To further an understanding of the nature of information available from Xe chemical shifts in cavities in biological systems, it would be advantageous to start with Xe in regular nanochannels that have well known ordered structures built from amino acid units. In this paper, we report the experimental observation of Xe NMR lineshapes in peptide channels, specifically the self-assembled nanochannels of the dipeptide L-Val-L-Ala and its retroanalog L-Ala-L-Val in the crystalline state. We carry out grand canonical Monte Carlo simulations of Xe in these channels to provide a physical understanding of the observed Xe lineshapes in these two systems.S elf-assembling structures with nanochannels have been of increasing interest (1, 2). A subset of these (peptide-based nanochannels) have demonstrated applicability as transmembrane pores and ion channels, as well as size-selective ion sensors (1). Görbitz and coworkers (3, 4) have described peptide nanochannels formed by the aggregation of dipeptides in a head-to-tail hydrogen-bonded network, forming a channel with a hydrophobic interior. Two such systems, the dipeptide L-Val-L-Ala (3) (VA) and its retroanalog, L-Ala-L-Val (4) (AV), form two distinct channels, which have been demonstrated to act as supramolecular hosts for organic molecules. These dipeptide systems are the subject of the present study.Binding of Xe within cavities in proteins is common because of several favorable factors. The Xe atom has a large electric dipole polarizability; cavities within proteins are about the correct size to hold one or more Xe atoms, and the unfavorable entropic term related to the need to orient the ligand in the binding site is absent for Xe atom. The affinity of Xe for hydrophobic cavities in the interiors of macromolecules (5-10) coupled with the development of techniques for hyperpolarization of Xe nuclear spins have inspired an array of NMR studies of Xe in proteins (11), cells, (12, 13), and tissues (14-16). For example, hyperpolarized (HP) 129 Xe has been developed as a tool for the characterization of protein cavities which bind Xe, by using its nuclear spin polarization to enhance the signals of the protons in the cavity (10, 17), by using the Xe chemical shift itself as a reporter of cavity structure in both solution and the solid state (11), and in applications to biomolecular assays (18,19).Xe adsorbed into nanochannels and cavities gives rise to an anisotropic lineshape in the NMR spectrum. Such lineshapes have been observed experimentally in 1D channels in various crystalline materials (20)(21)(22)(23), with the observed lineshape varying with changing Xe occupancy within the channel. A theoretical understanding, using the dimer tensor model in grand canonical Monte Carlo (GCMC) simulations (24), permits the prediction of the average Xe chemical shift tensor and the lineshapes that are observed in the Xe NMR spectrum of a polycrystalline sample (24, 25) or of a single crystal (26), with no adjustable parameters. The lineshapes calculated for a uniform distribution...